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Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)

 CDK1_HUMAN              Reviewed;         297 AA.
P06493; A8K7C4; C9J497; O60764;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 3.
12-AUG-2020, entry version 253.
RecName: Full=Cyclin-dependent kinase 1;
Short=CDK1;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=Cell division control protein 2 homolog;
AltName: Full=Cell division protein kinase 1;
AltName: Full=p34 protein kinase;
Name=CDK1; Synonyms=CDC2, CDC28A, CDKN1, P34CDC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3553962; DOI=10.1038/327031a0;
Lee M.G., Nurse P.;
"Complementation used to clone a human homologue of the fission yeast cell
cycle control gene cdc2.";
Nature 327:31-35(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Mammary cancer;
PubMed=9515786;
Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S.,
Xiong Y.;
"T-loop deletion of CDC2 from breast cancer tissues eliminates binding to
cyclin B1 and cyclin-dependent kinase inhibitor p21.";
Cancer Res. 58:1095-1098(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION, AND ASSOCIATION WITH P13.
PubMed=3289755; DOI=10.1016/0092-8674(88)90175-4;
Draetta G., Beach D.;
"Activation of cdc2 protein kinase during mitosis in human cells: cell
cycle-dependent phosphorylation and subunit rearrangement.";
Cell 54:17-26(1988).
[10]
PHOSPHORYLATION AT THR-14 AND TYR-15 BY PKMYT1.
PubMed=7569953; DOI=10.1126/science.270.5233.86;
Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G.;
"Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on
both threonine-14 and tyrosine-15.";
Science 270:86-90(1995).
[11]
INTERACTION WITH FANCC.
PubMed=9242535;
Kupfer G.M., Yamashita T., Naf D., Suliman A., Asano S., D'Andrea A.D.;
"The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase,
cdc2.";
Blood 90:1047-1054(1997).
[12]
ACTIVITY REGULATION BY ROSCOVITINE AND OLOMOUCINE.
PubMed=9030781; DOI=10.1111/j.1432-1033.1997.t01-2-00527.x;
Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N.,
Inagaki M., Delcros J.-G., Moulinoux J.-P.;
"Biochemical and cellular effects of roscovitine, a potent and selective
inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5.";
Eur. J. Biochem. 243:527-536(1997).
[13]
INTERACTION WITH RALBP1.
PubMed=12775724; DOI=10.1074/jbc.m302191200;
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
phosphorylate epsin during the switch off of endocytosis in mitosis.";
J. Biol. Chem. 278:30597-30604(2003).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[15]
INTERACTION WITH DLGAP5.
PubMed=15145941; DOI=10.1074/jbc.m404950200;
Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated
hepatoma up-regulated protein (HURP) proteolysis by a proline-rich
region.";
J. Biol. Chem. 279:32592-32602(2004).
[16]
FUNCTION AS RUNX2 KINASE.
PubMed=16407259; DOI=10.1074/jbc.m508162200;
Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.;
"Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by
cdc2 regulates endothelial cell proliferation.";
J. Biol. Chem. 281:7118-7128(2006).
[17]
FUNCTION AS BETA-TUBULINS KINASE.
PubMed=16371510; DOI=10.1091/mbc.e05-07-0621;
Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C.,
Lantez V., Job D.;
"Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-
dependent kinase Cdk1.";
Mol. Biol. Cell 17:1041-1050(2006).
[18]
INDUCTION BY CKS1B.
PubMed=18056467; DOI=10.1158/0008-5472.can-06-4173;
Westbrook L., Manuvakhova M., Kern F.G., Estes N.R. II, Ramanathan H.N.,
Thottassery J.V.;
"Cks1 regulates cdk1 expression: a novel role during mitotic entry in
breast cancer cells.";
Cancer Res. 67:11393-11401(2007).
[19]
FUNCTION AS RB1 KINASE, ACTIVITY REGULATION BY TGFB1, AND REPRESSION BY
TGFB1.
PubMed=17459720; DOI=10.1016/j.cyto.2007.03.009;
Hu X., Cui D., Moscinski L.C., Zhang X., Maccachero V., Zuckerman K.S.;
"TGFbeta regulates the expression and activities of G2 checkpoint kinases
in human myeloid leukemia cells.";
Cytokine 37:155-162(2007).
[20]
FUNCTION AS SIRT2 KINASE, AND SUBCELLULAR LOCATION.
PubMed=16933150; DOI=10.1007/s11064-006-9127-6;
Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.;
"Microtubule deacetylases, SirT2 and HDAC6, in the nervous system.";
Neurochem. Res. 32:187-195(2007).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
FUNCTION DURING THE M PHASE, AND MUTAGENESIS OF 14-THR-TYR-15.
PubMed=18480403; DOI=10.1091/mbc.e08-02-0172;
Pomerening J.R., Ubersax J.A., Ferrell J.E. Jr.;
"Rapid cycling and precocious termination of G1 phase in cells expressing
CDK1AF.";
Mol. Biol. Cell 19:3426-3441(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-39; TYR-77 AND
THR-222, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
FUNCTION AS FOXO1 KINASE, AND INTERACTION WITH FOXO1.
PubMed=18356527; DOI=10.1126/science.1152337;
Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y.,
Schaefer E.M., Bonni A.;
"Activation of FOXO1 by Cdk1 in cycling cells and postmitotic neurons.";
Science 319:1665-1668(2008).
[26]
FUNCTION AS NEDD1 KINASE.
PubMed=19509060; DOI=10.1242/jcs.042747;
Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.;
"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for
targeting of the gammaTuRC to the centrosome.";
J. Cell Sci. 122:2240-2251(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT TYR-19; SER-39; SER-178; THR-222 AND SER-248, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND THR-161, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[30]
FUNCTION AS CC2D1A KINASE.
PubMed=20171170; DOI=10.1016/j.bbrc.2010.02.103;
Nakamura A., Naito M., Arai H., Fujita N.;
"Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1 complex.";
Biochem. Biophys. Res. Commun. 393:872-876(2010).
[31]
FUNCTION IN G2 ARREST UPON DNA DAMAGE, PHOSPHORYLATION AT TYR-4 BY
PKR/EIF2AK2, POLYUBIQUITINATION, AND MUTAGENESIS OF TYR-4.
PubMed=20395957; DOI=10.1038/embor.2010.45;
Yoon C.-H., Miah M.A., Kim K.P., Bae Y.-S.;
"New Cdc2 Tyr 4 phosphorylation by dsRNA-activated protein kinase triggers
Cdc2 polyubiquitination and G2 arrest under genotoxic stresses.";
EMBO Rep. 11:393-399(2010).
[32]
PHOSPHORYLATION AT TYR-15.
PubMed=19917613; DOI=10.1074/jbc.m109.055392;
LaGory E.L., Sitailo L.A., Denning M.F.;
"The protein kinase Cdelta catalytic fragment is critical for maintenance
of the G2/M DNA damage checkpoint.";
J. Biol. Chem. 285:1879-1887(2010).
[33]
FUNCTION IN G2-M TRANSITION, DEPHOSPHORYLATION AT THR-14 AND TYR-15 BY
CDC25, PHOSPHORYLATION AT THR-161 BY CDK7/CAK, AND INTERACTION WITH
B-CYCLIN.
PubMed=20360007; DOI=10.1074/jbc.m109.096552;
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.;
"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at
the G2/M transition.";
J. Biol. Chem. 285:16978-16990(2010).
[34]
FUNCTION AS BCL-XL/BCL2L1 KINASE, AND SUBCELLULAR LOCATION.
PubMed=19917720; DOI=10.1128/mcb.00882-09;
Terrano D.T., Upreti M., Chambers T.C.;
"Cyclin-dependent kinase 1-mediated Bcl-xL/Bcl-2 phosphorylation acts as a
functional link coupling mitotic arrest and apoptosis.";
Mol. Cell. Biol. 30:640-656(2010).
[35]
FUNCTION AS CASP8 KINASE.
PubMed=20937773; DOI=10.1128/mcb.00731-10;
Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.;
"Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8
activity.";
Mol. Cell. Biol. 30:5726-5740(2010).
[36]
FUNCTION AS EZH2 KINASE.
PubMed=20935635; DOI=10.1038/ncb2116;
Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A.,
Simon J.A., Huang H.;
"Cyclin-dependent kinases regulate epigenetic gene silencing through
phosphorylation of EZH2.";
Nat. Cell Biol. 12:1108-1114(2010).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION.
PubMed=21406398; DOI=10.1158/0008-5472.can-10-2684;
Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M.,
Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.;
"Cep63 recruits Cdk1 to the centrosome: implications for regulation of
mitotic entry, centrosome amplification, and genome maintenance.";
Cancer Res. 71:2129-2139(2011).
[40]
FUNCTION AS CHAMP1 KINASE.
PubMed=21063390; DOI=10.1038/emboj.2010.276;
Itoh G., Kanno S., Uchida K.S., Chiba S., Sugino S., Watanabe K.,
Mizuno K., Yasui A., Hirota T., Tanaka K.;
"CAMP (C13orf8, ZNF828) is a novel regulator of kinetochore-microtubule
attachment.";
EMBO J. 30:130-144(2011).
[41]
REVIEW ON SUBSTRATES, AND GENE FAMILY.
PubMed=16236519; DOI=10.1016/j.tibs.2005.09.005;
Malumbres M., Barbacid M.;
"Mammalian cyclin-dependent kinases.";
Trends Biochem. Sci. 30:630-641(2005).
[42]
REVIEW ON SUBCELLULAR TRANSLOCATION.
PubMed=19364923; DOI=10.1083/jcb.200812045;
Lindqvist A., Rodriguez-Bravo V., Medema R.H.;
"The decision to enter mitosis: feedback and redundancy in the mitotic
entry network.";
J. Cell Biol. 185:193-202(2009).
[43]
REVIEW ON CELL CYCLE CONTROL AND INHIBITORS, AND GENE FAMILY.
PubMed=19238148; DOI=10.1038/nrc2602;
Malumbres M., Barbacid M.;
"Cell cycle, CDKs and cancer: a changing paradigm.";
Nat. Rev. Cancer 9:153-166(2009).
[44]
REVIEW ON CELL CYCLE CONTROL.
PubMed=21535261; DOI=10.1111/j.1365-2184.2011.00753.x;
Hu X., Moscinski L.C.;
"Cdc2: a monopotent or pluripotent CDK?";
Cell Prolif. 44:205-211(2011).
[45]
REVIEW ON CELL CYCLE CONTROL AND INHIBITORS.
PubMed=21517772; DOI=10.2174/092986711795590110;
Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.;
"Cyclin dependent kinase 1 inhibitors: a review of recent progress.";
Curr. Med. Chem. 18:2025-2043(2011).
[46]
REVIEW ON CELL CYCLE CONTROL.
PubMed=21655336; DOI=10.3410/b3-10;
Medema R.H., Macurek L.;
"Checkpoint recovery in cells: how a molecular understanding can help in
the fight against cancer.";
F1000 Biol. Rep. 3:10-10(2011).
[47]
FUNCTION (MICROBIAL INFECTION).
PubMed=21516087; DOI=10.1038/nm.2341;
Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B., Zahid M.N.,
Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M., Pietschmann T.,
Patel A.H., Pessaux P., Doffoel M., Raffelsberger W., Poch O.,
McKeating J.A., Brino L., Baumert T.F.;
"EGFR and EphA2 are host factors for hepatitis C virus entry and possible
targets for antiviral therapy.";
Nat. Med. 17:589-595(2011).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[50]
FUNCTION.
PubMed=23602554; DOI=10.1016/j.celrep.2013.03.017;
Cribier A., Descours B., Valadao A.L., Laguette N., Benkirane M.;
"Phosphorylation of SAMHD1 by cyclin A2/CDK1 regulates its restriction
activity toward HIV-1.";
Cell Rep. 3:1036-1043(2013).
[51]
FUNCTION.
PubMed=23601106; DOI=10.1016/j.chom.2013.03.005;
White T.E., Brandariz-Nunez A., Valle-Casuso J.C., Amie S., Nguyen L.A.,
Kim B., Tuzova M., Diaz-Griffero F.;
"The retroviral restriction ability of SAMHD1, but not its deoxynucleotide
triphosphohydrolase activity, is regulated by phosphorylation.";
Cell Host Microbe 13:441-451(2013).
[52]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=23355470; DOI=10.1074/jbc.m112.441048;
Schofield A.V., Gamell C., Suryadinata R., Sarcevic B., Bernard O.;
"Tubulin polymerization promoting protein 1 (Tppp1) phosphorylation by Rho-
associated coiled-coil kinase (rock) and cyclin-dependent kinase 1 (Cdk1)
inhibits microtubule dynamics to increase cell proliferation.";
J. Biol. Chem. 288:7907-7917(2013).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; THR-141 AND THR-161, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[54]
FUNCTION.
PubMed=26549230; DOI=10.1016/j.bbrc.2015.11.004;
Mori Y., Inoue Y., Taniyama Y., Tanaka S., Terada Y.;
"Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its
dissociation from centrosomes in mitosis.";
Biochem. Biophys. Res. Commun. 468:642-646(2015).
[55]
FUNCTION, AND INTERACTION WITH CENPA.
PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030;
Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S., Cui L.,
Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G., Zhang X.,
Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
"Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-cycle-
dependent deposition at centromeres.";
Dev. Cell 32:68-81(2015).
[56]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[57]
FUNCTION, AND INTERACTION WITH NR1D1.
PubMed=27238018; DOI=10.1016/j.cell.2016.05.012;
Zhao X., Hirota T., Han X., Cho H., Chong L.W., Lamia K., Liu S.,
Atkins A.R., Banayo E., Liddle C., Yu R.T., Yates J.R. III, Kay S.A.,
Downes M., Evans R.M.;
"Circadian amplitude regulation via FBXW7-targeted REV-ERBalpha
degradation.";
Cell 165:1644-1657(2016).
[58]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-20 AND LYS-139, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle
by modulating the centrosome cycle as well as mitotic onset; promotes
G2-M transition, and regulates G1 progress and G1-S transition via
association with multiple interphase cyclins. Required in higher cells
for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin,
APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20,
CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7,
CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5,
EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1
proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1,
MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear
pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1,
PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA,
PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1,
KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins,
MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2
and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase
fertilized eggs. Essential for early stages of embryonic development.
During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation
activates CDK1/cyclin complexes which phosphorylate several substrates
that trigger at least centrosome separation, Golgi dynamics, nuclear
envelope breakdown and chromosome condensation. Once chromosomes are
condensed and aligned at the metaphase plate, CDK1 activity is switched
off by WEE1- and PKMYT1-mediated phosphorylation to allow sister
chromatid separation, chromosome decondensation, reformation of the
nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-
mediated phosphorylation upon DNA damage to stop cell cycle and genome
replication at the G2 checkpoint thus facilitating DNA repair.
Reactivated after successful DNA repair through WIP1-dependent
signaling leading to CDC25A/B/C-mediated dephosphorylation and
restoring cell cycle progression. In proliferating cells, CDK1-mediated
FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction
with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation
and transcription factor activity, leading to cell death of postmitotic
neurons. The phosphorylation of beta-tubulins regulates microtubule
dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated
NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin
ring complex (gTuRC) to the centrosome, an important step for spindle
formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle
pole localization and association with SCC1/RAD21 and centriole
cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after
prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast,
CASP8 phosphorylation during mitosis prevents its activation by
proteolysis and subsequent apoptosis. This phosphorylation occurs in
cancer cell lines, as well as in primary breast tissues and
lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and
epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell
migration during peripheral nerve regeneration. CDK1-cyclin-B complex
phosphorylates NCKAP5L and mediates its dissociation from centrosomes
during mitosis (PubMed:26549230). Regulates the amplitude of the cyclic
expression of the core clock gene ARNTL/BMAL1 by phosphorylating its
transcriptional repressor NR1D1, and this phosphorylation is necessary
for SCF(FBXW7)-mediated ubiquitination and proteasomal degradation of
NR1D1 (PubMed:27238018). {ECO:0000269|PubMed:16371510,
ECO:0000269|PubMed:16407259, ECO:0000269|PubMed:16933150,
ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18356527,
ECO:0000269|PubMed:18480403, ECO:0000269|PubMed:19509060,
ECO:0000269|PubMed:19917720, ECO:0000269|PubMed:20171170,
ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:20395957,
ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:20937773,
ECO:0000269|PubMed:21063390, ECO:0000269|PubMed:23355470,
ECO:0000269|PubMed:23601106, ECO:0000269|PubMed:23602554,
ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:26549230,
ECO:0000269|PubMed:27238018}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
virus (HCV) in hepatocytes and facilitates its cell entry.
{ECO:0000269|PubMed:21516087}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
Evidence={ECO:0000269|PubMed:23355470};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.22; Evidence={ECO:0000269|PubMed:23355470};
-!- CATALYTIC ACTIVITY:
Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
ChEBI:CHEBI:456216; EC=2.7.11.23;
-!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
the enzyme, while phosphorylation at Thr-161 activates it. Activated
through a multistep process; binding to cyclin-B is required for
relocation of cyclin-kinase complexes to the nucleus, activated by
CAK/CDK7-mediated phosphorylation on Thr-161, and CDC25-mediated
dephosphorylation of inhibitory phosphorylation on Thr-14 and Tyr-15.
Inhibited by flavopiridol and derivatives, pyrimidine derivatives,
pyridine derivatives, purine derivatives, staurosporine, paullones,
oxoindoles, indazole analogs, indolin-2-ones, pyrazolo[3,4-b]pyridines,
imidazo[1,2-a]pyridine (AZ703), thiazolinone analogs(RO-3306), thiazol
urea, macrocyclic quinoxalin-2-one, pyrrolo[2,3-a]carbazole,
pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine (Dinaciclib,
SCH 727965), 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-
isopropylpurine (roscovitine), olomoucine, AG-024322, AT-7519, P276-00,
R547/Ro-4584820 and SNS-032/BMS-387032. Repressed by the CDK inhibitors
CDKN1A/p21 and CDKN1B/p27 during the G1 phase and by CDKN1A/p21 at the
G1-S checkpoint upon DNA damage. Transient activation by rapid and
transient dephosphorylation at Tyr-15 triggered by TGFB1.
{ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:9030781}.
-!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
subunit and with a cyclin. Interacts with cyclins-B (CCNB1, CCNB2 and
CCNB3) to form a serine/threonine kinase holoenzyme complex also known
as maturation promoting factor (MPF). The cyclin subunit imparts
substrate specificity to the complex. Can also form CDK1-cylin-D and
CDK1-cyclin-E complexes that phosphorylate RB1 in vitro. Binds to RB1
and other transcription factors such as FOXO1 and RUNX2. Promotes G2-M
transition when in complex with a cyclin-B. Interacts with DLGAP5.
Binds to the CDK inhibitors CDKN1A/p21 and CDKN1B/p27. Isoform 2 is
unable to complex with cyclin-B1 and also fails to bind to CDKN1A/p21.
Interacts with catalytically active CCNB1 and RALBP1 during mitosis to
form an endocytotic complex during interphase. Associates with cyclins-
A and B1 during S-phase in regenerating hepatocytes. Interacts with
FANCC. Interacts with CEP63; this interaction recruits CDK1 to
centrosomes. Interacts with CENPA (PubMed:25556658). Interacts with
NR1D1 (PubMed:27238018). Interacts with proteasome subunit PSMA8; to
participate in meiosis progression during spermatogenesis (By
similarity). {ECO:0000250|UniProtKB:P11440,
ECO:0000269|PubMed:12775724, ECO:0000269|PubMed:15145941,
ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:20360007,
ECO:0000269|PubMed:21406398, ECO:0000269|PubMed:25556658,
ECO:0000269|PubMed:27238018, ECO:0000269|PubMed:9242535}.
-!- INTERACTION:
P06493; Q86V81: ALYREF; NbExp=4; IntAct=EBI-444308, EBI-347640;
P06493; O15392: BIRC5; NbExp=6; IntAct=EBI-444308, EBI-518823;
P06493; P14635: CCNB1; NbExp=20; IntAct=EBI-444308, EBI-495332;
P06493; P30307: CDC25C; NbExp=2; IntAct=EBI-444308, EBI-974439;
P06493; Q99741: CDC6; NbExp=2; IntAct=EBI-444308, EBI-374862;
P06493; P38936: CDKN1A; NbExp=5; IntAct=EBI-444308, EBI-375077;
P06493; P61024: CKS1B; NbExp=9; IntAct=EBI-444308, EBI-456371;
P06493; O75618-1: DEDD; NbExp=2; IntAct=EBI-444308, EBI-15621191;
P06493; P36957: DLST; NbExp=3; IntAct=EBI-444308, EBI-351007;
P06493; P00533: EGFR; NbExp=3; IntAct=EBI-444308, EBI-297353;
P06493; P19525: EIF2AK2; NbExp=4; IntAct=EBI-444308, EBI-640775;
P06493; Q12778: FOXO1; NbExp=5; IntAct=EBI-444308, EBI-1108782;
P06493; O95835: LATS1; NbExp=3; IntAct=EBI-444308, EBI-444209;
P06493; Q99640: PKMYT1; NbExp=5; IntAct=EBI-444308, EBI-495308;
P06493; P0CG48: UBC; NbExp=6; IntAct=EBI-444308, EBI-3390054;
P06493; P03070; Xeno; NbExp=2; IntAct=EBI-444308, EBI-617698;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:14654843}. Cytoplasm, cytoskeleton, spindle.
Note=Cytoplasmic during the interphase. Colocalizes with SIRT2 on
centrosome during prophase and on splindle fibers during metaphase of
the mitotic cell cycle. Reversibly translocated from cytoplasm to
nucleus when phosphorylated before G2-M transition when associated with
cyclin-B1. Accumulates in mitochondria in G2-arrested cells upon DNA-
damage.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P06493-1; Sequence=Displayed;
Name=2; Synonyms=CDC2deltaT;
IsoId=P06493-2; Sequence=VSP_021375;
-!- TISSUE SPECIFICITY: Isoform 2 is found in breast cancer tissues.
-!- INDUCTION: Follows a cyclic expression; during interphase, accumulates
gradually following G1, S to reach a critical threshold at the end of
G2, which promotes self-activation and triggers onset of mitosis.
Induced transiently by TGFB1 at an early phase of TGFB1-mediated
apoptosis, but later repressed. Triggered by CKS1B during mitotic entry
in breast cancer cells. Down-regulated under genotoxic stresses
triggered by PKR/EIF2AK2-mediated phosphorylation.
{ECO:0000269|PubMed:17459720, ECO:0000269|PubMed:18056467}.
-!- PTM: Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity.
Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear
translocation. Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the
protein kinase activity and acts as a negative regulator of entry into
mitosis (G2 to M transition). Phosphorylation by PKMYT1 and WEE1 takes
place during mitosis to keep CDK1-cyclin-B complexes inactive until the
end of G2. By the end of G2, PKMYT1 and WEE1 are inactivated, but
CDC25A and CDC25B are activated. Dephosphorylation by active CDC25A and
CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M
transition. Phosphorylation at Tyr-15 by WEE2 during oogenesis is
required to maintain meiotic arrest in oocytes during the germinal
vesicle (GV) stage, a long period of quiescence at dictyate prophase I,
leading to prevent meiotic reentry. Phosphorylation by WEE2 is also
required for metaphase II exit during egg activation to ensure exit
from meiosis in oocytes and promote pronuclear formation.
Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress. This
phosphorylation triggers CDK1 polyubiquitination and subsequent
proteolysis, thus leading to G2 arrest. In response to UV irradiation,
phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage
checkpoint. {ECO:0000269|PubMed:19917613, ECO:0000269|PubMed:20360007,
ECO:0000269|PubMed:20395957, ECO:0000269|PubMed:3289755,
ECO:0000269|PubMed:7569953}.
-!- PTM: Polyubiquitinated upon genotoxic stress.
{ECO:0000269|PubMed:20395957}.
-!- MISCELLANEOUS: As a key regulator of the cell cycle, CDK1 is a potent
therapeutic target for inhibitors in cancer treatment.
{ECO:0000305|PubMed:21517772}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAW54204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc2/";
---------------------------------------------------------------------------
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EMBL; X05360; CAA28963.1; -; mRNA.
EMBL; Y00272; CAA68376.1; -; mRNA.
EMBL; D88357; BAA26001.1; -; mRNA.
EMBL; AK291939; BAF84628.1; -; mRNA.
EMBL; BT007004; AAP35650.1; -; mRNA.
EMBL; AF512554; AAM34793.1; -; Genomic_DNA.
EMBL; AC022390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54204.1; ALT_SEQ; Genomic_DNA.
EMBL; BC014563; AAH14563.1; -; mRNA.
CCDS; CCDS44408.1; -. [P06493-1]
CCDS; CCDS7260.1; -. [P06493-2]
PIR; A29539; A29539.
RefSeq; NP_001307847.1; NM_001320918.1. [P06493-1]
RefSeq; NP_001777.1; NM_001786.4. [P06493-1]
RefSeq; NP_203698.1; NM_033379.4. [P06493-2]
RefSeq; XP_005270360.1; XM_005270303.3. [P06493-1]
PDB; 1LC9; Model; -; A=1-297.
PDB; 4Y72; X-ray; 2.30 A; A=1-297.
PDB; 4YC3; X-ray; 2.70 A; A=1-297.
PDB; 4YC6; X-ray; 2.60 A; A/C/E/G=1-297.
PDB; 5HQ0; X-ray; 2.30 A; A=1-297.
PDB; 5LQF; X-ray; 2.06 A; A/D=1-297.
PDB; 6GU2; X-ray; 2.00 A; A=1-297.
PDB; 6GU3; X-ray; 2.65 A; A=1-297.
PDB; 6GU4; X-ray; 2.73 A; A=1-297.
PDB; 6GU6; X-ray; 2.33 A; A=1-297.
PDB; 6GU7; X-ray; 2.75 A; A/C/E/G=1-297.
PDBsum; 1LC9; -.
PDBsum; 4Y72; -.
PDBsum; 4YC3; -.
PDBsum; 4YC6; -.
PDBsum; 5HQ0; -.
PDBsum; 5LQF; -.
PDBsum; 6GU2; -.
PDBsum; 6GU3; -.
PDBsum; 6GU4; -.
PDBsum; 6GU6; -.
PDBsum; 6GU7; -.
SMR; P06493; -.
BioGRID; 107420; 328.
ComplexPortal; CPX-2003; Cyclin A1-CDK1 complex.
ComplexPortal; CPX-2004; Cyclin A2-CDK1 complex.
ComplexPortal; CPX-2007; Cyclin B1-CDK1 complex.
ComplexPortal; CPX-2008; Cyclin B2-CDK1 complex.
CORUM; P06493; -.
DIP; DIP-35N; -.
ELM; P06493; -.
IntAct; P06493; 158.
MINT; P06493; -.
STRING; 9606.ENSP00000378699; -.
BindingDB; P06493; -.
ChEMBL; CHEMBL308; -.
DrugBank; DB04014; Alsterpaullone.
DrugBank; DB03496; Alvocidib.
DrugBank; DB08142; AT-7519.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB02950; Hymenialdisine.
DrugBank; DB02052; Indirubin-3'-monoxime.
DrugBank; DB02116; Olomoucine.
DrugBank; DB06195; Seliciclib.
DrugBank; DB03428; SU9516.
DrugCentral; P06493; -.
GuidetoPHARMACOLOGY; 1961; -.
TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
iPTMnet; P06493; -.
MetOSite; P06493; -.
PhosphoSitePlus; P06493; -.
SwissPalm; P06493; -.
BioMuta; CDK1; -.
DMDM; 334302921; -.
SWISS-2DPAGE; P06493; -.
CPTAC; CPTAC-1040; -.
CPTAC; CPTAC-1041; -.
CPTAC; CPTAC-1042; -.
CPTAC; CPTAC-1200; -.
CPTAC; CPTAC-797; -.
CPTAC; CPTAC-798; -.
CPTAC; CPTAC-801; -.
EPD; P06493; -.
jPOST; P06493; -.
MassIVE; P06493; -.
MaxQB; P06493; -.
PaxDb; P06493; -.
PeptideAtlas; P06493; -.
PRIDE; P06493; -.
ProteomicsDB; 51905; -. [P06493-1]
ProteomicsDB; 51906; -. [P06493-2]
Antibodypedia; 1134; 2606 antibodies.
DNASU; 983; -.
Ensembl; ENST00000316629; ENSP00000325970; ENSG00000170312. [P06493-2]
Ensembl; ENST00000373809; ENSP00000362915; ENSG00000170312. [P06493-2]
Ensembl; ENST00000395284; ENSP00000378699; ENSG00000170312. [P06493-1]
GeneID; 983; -.
KEGG; hsa:983; -.
UCSC; uc001jld.3; human. [P06493-1]
CTD; 983; -.
DisGeNET; 983; -.
EuPathDB; HostDB:ENSG00000170312.15; -.
GeneCards; CDK1; -.
HGNC; HGNC:1722; CDK1.
HPA; ENSG00000170312; Tissue enriched (lymphoid).
MIM; 116940; gene.
neXtProt; NX_P06493; -.
OpenTargets; ENSG00000170312; -.
PharmGKB; PA99; -.
eggNOG; KOG0594; Eukaryota.
GeneTree; ENSGT00940000153335; -.
HOGENOM; CLU_000288_181_6_1; -.
InParanoid; P06493; -.
KO; K02087; -.
OMA; MTHPYFD; -.
OrthoDB; 286319at2759; -.
PhylomeDB; P06493; -.
TreeFam; TF101021; -.
BRENDA; 2.7.11.22; 2681.
PathwayCommons; P06493; -.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-170145; Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-176417; Phosphorylation of Emi1.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-68875; Mitotic Prophase.
Reactome; R-HSA-69205; G1/S-Specific Transcription.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69478; G2/M DNA replication checkpoint.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
SignaLink; P06493; -.
SIGNOR; P06493; -.
BioGRID-ORCS; 983; 774 hits in 884 CRISPR screens.
ChiTaRS; CDK1; human.
GeneWiki; Cdk1; -.
GeneWiki; Cyclin-dependent_kinase_1; -.
GenomeRNAi; 983; -.
Pharos; P06493; Tchem.
PRO; PR:P06493; -.
Proteomes; UP000005640; Chromosome 10.
RNAct; P06493; protein.
Bgee; ENSG00000170312; Expressed in ventricular zone and 185 other tissues.
ExpressionAtlas; P06493; baseline and differential.
Genevisible; P06493; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097125; C:cyclin B1-CDK1 complex; IMP:CAFA.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0030332; F:cyclin binding; IDA:MGI.
GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0035173; F:histone kinase activity; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; TAS:UniProtKB.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0007098; P:centrosome cycle; TAS:UniProtKB.
GO; GO:0030261; P:chromosome condensation; IEA:Ensembl.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:UniProtKB.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IBA:GO_Central.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:CAFA.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; IMP:CAFA.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
GO; GO:0007344; P:pronuclear fusion; TAS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0034501; P:protein localization to kinetochore; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0045995; P:regulation of embryonic development; TAS:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0014038; P:regulation of Schwann cell differentiation; TAS:UniProtKB.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Biological rhythms; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
Host cell receptor for virus entry; Host-virus interaction;
Isopeptide bond; Kinase; Mitochondrion; Mitosis; Nucleotide-binding;
Nucleus; Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1..297
/note="Cyclin-dependent kinase 1"
/id="PRO_0000085724"
DOMAIN 4..287
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 10..18
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 128
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 33
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22814378"
MOD_RES 4
/note="Phosphotyrosine; by PKR"
/evidence="ECO:0000269|PubMed:20395957"
MOD_RES 6
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 9
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P11440"
MOD_RES 14
/note="Phosphothreonine; by PKMYT1"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000269|PubMed:7569953"
MOD_RES 15
/note="Phosphotyrosine; by PKMYT1, WEE1, WEE2 and
PKC/PRKCD"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000269|PubMed:19917613,
ECO:0000269|PubMed:7569953"
MOD_RES 19
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES 39
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:23186163"
MOD_RES 77
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:18691976"
MOD_RES 141
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 161
/note="Phosphothreonine; by CAK"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:20360007"
MOD_RES 178
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 222
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195"
MOD_RES 245
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P11440"
MOD_RES 248
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
CROSSLNK 6
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 9
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 20
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 139
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
VAR_SEQ 107..163
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:9515786"
/id="VSP_021375"
MUTAGEN 4
/note="Y->D,E: Constitutive polyubiquitination."
/evidence="ECO:0000269|PubMed:20395957"
MUTAGEN 14..15
/note="TY->AF: Abnormal cell cycle exhibiting only M-phase
without completing either karyokinesis or cytokinesis."
/evidence="ECO:0000269|PubMed:18480403"
HELIX 1..3
/evidence="ECO:0000244|PDB:6GU2"
STRAND 4..13
/evidence="ECO:0000244|PDB:6GU2"
STRAND 16..23
/evidence="ECO:0000244|PDB:6GU2"
TURN 24..26
/evidence="ECO:0000244|PDB:6GU2"
STRAND 29..35
/evidence="ECO:0000244|PDB:6GU2"
HELIX 40..42
/evidence="ECO:0000244|PDB:6GU2"
HELIX 46..57
/evidence="ECO:0000244|PDB:6GU2"
STRAND 66..72
/evidence="ECO:0000244|PDB:6GU2"
STRAND 75..81
/evidence="ECO:0000244|PDB:6GU2"
STRAND 84..86
/evidence="ECO:0000244|PDB:5LQF"
HELIX 87..93
/evidence="ECO:0000244|PDB:6GU2"
HELIX 102..120
/evidence="ECO:0000244|PDB:6GU2"
TURN 121..123
/evidence="ECO:0000244|PDB:6GU2"
HELIX 131..133
/evidence="ECO:0000244|PDB:6GU2"
STRAND 134..136
/evidence="ECO:0000244|PDB:6GU2"
STRAND 142..144
/evidence="ECO:0000244|PDB:6GU2"
HELIX 149..152
/evidence="ECO:0000244|PDB:6GU6"
STRAND 155..158
/evidence="ECO:0000244|PDB:6GU2"
TURN 161..163
/evidence="ECO:0000244|PDB:4YC6"
HELIX 164..167
/evidence="ECO:0000244|PDB:6GU6"
HELIX 172..175
/evidence="ECO:0000244|PDB:6GU2"
STRAND 179..181
/evidence="ECO:0000244|PDB:4YC6"
HELIX 184..199
/evidence="ECO:0000244|PDB:6GU2"
HELIX 209..220
/evidence="ECO:0000244|PDB:6GU2"
TURN 225..227
/evidence="ECO:0000244|PDB:6GU2"
HELIX 231..233
/evidence="ECO:0000244|PDB:6GU2"
HELIX 249..251
/evidence="ECO:0000244|PDB:6GU2"
HELIX 258..267
/evidence="ECO:0000244|PDB:6GU2"
TURN 272..274
/evidence="ECO:0000244|PDB:6GU2"
HELIX 278..282
/evidence="ECO:0000244|PDB:6GU2"
HELIX 285..287
/evidence="ECO:0000244|PDB:6GU2"
HELIX 292..295
/evidence="ECO:0000244|PDB:4YC3"
SEQUENCE 297 AA; 34095 MW; 942D79448EFE490A CRC64;
MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH
PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKSYLY QILQGIVFCH
SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR
YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT
FPKWKPGSLA SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM


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WP840: G1 to S cell cycle control
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WP1676: Non-homologous end-joining
WP1625: Base excision repair
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Related Genes :
[Cdk1 cdc2 CG5363] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[cdk1 cdcB DDB_G0272813] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[cdk1-b cdc2 cdc2x1.2] Cyclin-dependent kinase 1-B (CDK1-B) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 2) (Cell division control protein 2-B) (Cell division protein kinase 1) (p34 protein kinase 2)
[cdk1-a cdc2-a cdc2x1.1] Cyclin-dependent kinase 1-A (CDK1-A) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 1) (Cell division control protein 2-A) (Cell division protein kinase 1-A) (p34 protein kinase 1)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[cdc2 cdk1 swo2 pi002 SPBC11B10.09] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[cdk1 cdc2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[cdk1 cdc2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[nimX cdk1 AN4182] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (Never in mitosis protein X)
[cdk1 cdc2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDC28 CDK1 CAALFM_CR06050WA CaO19.11337 CaO19.3856] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 2)
[CDC28 CDK1 HSL5 SRM5 YBR160W YBR1211] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 1)
[cdk1 cdc2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[cdk1 cdc2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDKA-1 CDC2 CDC2A At3g48750 T21J18.20] Cyclin-dependent kinase A-1 (CDKA;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog A) (CDC2aAt)
[CDK7 CAK CAK1 CDKN7 MO15 STK1] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (p39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (Serine/threonine-protein kinase 1) (TFIIH basal transcription factor complex kinase subunit)
[CDK2 CDKN2] Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2) (p33 protein kinase)
[CDKB1-1 CDC2B At3g54180 F24B22.140] Cyclin-dependent kinase B1-1 (CDKB1;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog B)
[Cdk7 Cak Cak1 Mo15] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 protein kinase) (P39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (TFIIH basal transcription factor complex kinase subunit) (Fragment)
[Cdk7 Cak Cdkn7 Crk4 Mo15 Mpk-7] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (P39 Mo15) (CDK-activating kinase) (CR4 protein kinase) (CRK4) (Cell division protein kinase 7) (Protein-tyrosine kinase MPK-7) (TFIIH basal transcription factor complex kinase subunit)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[Cdk2 Cdkn2] Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2)
[CDK2 CDKN7] Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2)

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[32518258] CYCLIN-B1/2 and -D1 act in opposition to coordinate cortical progenitor self-renewal and lineage commitment.
[32516310] ULK1-ATG13 and their mitotic phospho-regulation by CDK1 connect autophagy to cell cycle.
[32516305] Mitotic phosphorylation of the ULK complex regulates cell cycle progression.
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[32324833] Ribosome binding protein GCN1 regulates the cell cycle and cell proliferation and is essential for the embryonic development of mice.
[32313933] EXOSC10 sculpts the transcriptome during the growth-to-maturation transition in mouse oocytes.
[32267835] YTHDF2 promotes mitotic entry and is regulated by cell cycle mediators.
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[32240602] Cdk1 Controls Global Epigenetic Landscape in Embryonic Stem Cells.